Florian Wilfling: Mechanisms of Cellular Quality Control
Research in our group interdisciplinary combines advanced live-cell microscopy, in situ correlative cryo-electron tomography, state-of-the-art quantitative mass spectrometry and unbiased system-wide approaches to study fundamental principles of protein homeostasis and their misregulation in aging and age-related diseases.
Proteins are the workhorses of cells and perform a vast array of functions. Often this requires the formation of large multi-protein complexes which act as a macromolecular machine for individual tasks. Recent technological advancements in structural biology have elucidated many aspects of the complex assembly and function of these machines. However, relatively little is known how disused, damaged or misassembled macromolecular protein complexes are disposed. Our main goal is to systematically identify quality control signals and factors important for surveillance of the assembly and functional state of macromolecular assemblies. For this we integrate a diverse set of techniques including biochemistry, advanced live-cell microscopy, correlative cryo-electron tomography, state-of-the-art quantitative mass spectrometry and unbiased system-wide approaches.
How to join the Lab
Currently there are opportunities to join our research group as a postdoctoral researcher.
Are you motivated to work on cutting-edge research projects collaboratively in an international team? Please apply by contacting Florian by email (Florian.Wilfling@biophys.mpg.de) and attach your CV and a brief motivation letter describing your background and particular research interests. We also encourage the candidates to develop their own ideas. Experience with electron microscopy, fluorescence microscopy, data analysis, biochemistry, cell biology is beneficial, but we also welcome interdisciplinary backgrounds (computational science, chemistry, biophysics).
- Wilfling F., Lee C.W. , Erdmann P.S., Zheng Y., Jentsch S., Pfander B., Schulman B.A. and Baumeister W. A selective autophagy pathway for phase separated endocytic protein deposits. Molecular Cell (2020) doi: 10.1016/j.molcel.2020.10.030
- Allegretti M., Zimmerli C.E., Rantos V., Wilfling F., Ronchi P., Fung H.K.H., Lee C.W., Hagen W., Turonova B., Karius K., Zhang X., Müller C., Schwab Y., Mahamid J., Pfander B., Kosinski J. and Beck M. In cell architecture of the nuclear pore complex and snapshots of its turnover. Nature 2020 doi: 10.1038/s41586-020-2670-5
- Lee C.W., Wilfling F., Ronchi P., Allegretti M., Mosalaganti S., Jentsch S., Beck M. and Pfander B. Selective autophagy degrades nuclear pore complexes. Nature Cell Biology 2020 Feb 06, 22;159–166(2020). doi: 10.1038/s41556-019-0459-2
- Wilfling F., Thiam A.R., Olarte M.J., Wang J., Beck R., Gould T.J., Allgeyer E.S., Pincet F., Bewersdorf J., Farese Jr. R.V.. and Walther T.C. Arf1/COPI machinery acts directly on lipid droplets and enables their connection to the ER for protein targeting. eLife 2014 Feb 04, 2014;3:e01607 doi: 10.7554/eLife.01607
- Wilfling F., Wang H., Haas J.T., Krahmer N., Gould T.J., Uchida A., Cheng J.X., Graham M., Christiano R., Fröhlich F., Liu X., Buhman K.K., Coleman R.A., Bewersdorf J., Farese Jr. R.V., and Walther T.C. Triacylglycerol Synthesis Enzymes Mediate Lipid Droplet Growth by Relocalizing from the ER to Lipid Droplets. Developmental Cell 2013 Feb 25; 24(4):384-99 doi: 10.1016/j.devcel.2013.01.013